Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 464, Issue 1, Pages 70-75Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.05.105
Keywords
DAPK2; Apoptosis; 14-3-3; Akt
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [23780106]
- Awa Bank Science and Culture Foundation of Tokushima
- Grants-in-Aid for Scientific Research [23780106, 13J08248] Funding Source: KAKEN
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Death-associated protein kinase 2 (DAPK2), a Ca2+/calmodulin-regulated serine/threonine kinase, induces apoptosis. However, the signaling mechanisms involved in this process are unknown. Using a proteomic approach, we identified 14-3-3 proteins as novel DAPK2-interacting proteins. The 14-3-3 family has the ability to bind to phosphorylated proteins via recognition of three conserved amino acid motifs (mode 1-3 motifs), and DAPK2 contains the mode 3 motif ((pS/pT)X1-2-COOH). The interaction of 14-3-3 proteins with DAPK2 was dependent on the phosphorylation of Thr(369), and effectively suppressed DAPK2 kinase activity and DAPK2-induced apoptosis. Furthermore, we revealed that the 14-3-3 binding site Thr(369) of DAPK2 was phosphorylated by the survival kinase Akt. Our findings suggest that DAPK2-induced apoptosis is negatively regulated by Akt and 14-3-3 proteins. (C) 2015 Elsevier Inc. All rights reserved.
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